The post-translational modification landscape of commercial beers
Abstract Beer is one of the most popular beverages worldwide. As a product of variable agricultural ingredients and processes, beer has high molecular complexity. We used DIA/SWATH-MS to investigate the proteomic complexity and diversity of 23 commercial Australian beers. While the overall complexit...
Guardado en:
Autores principales: | , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/c9d97b75257f40a181f8c3b9b9042c3e |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:c9d97b75257f40a181f8c3b9b9042c3e |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:c9d97b75257f40a181f8c3b9b9042c3e2021-12-02T17:06:09ZThe post-translational modification landscape of commercial beers10.1038/s41598-021-95036-02045-2322https://doaj.org/article/c9d97b75257f40a181f8c3b9b9042c3e2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-95036-0https://doaj.org/toc/2045-2322Abstract Beer is one of the most popular beverages worldwide. As a product of variable agricultural ingredients and processes, beer has high molecular complexity. We used DIA/SWATH-MS to investigate the proteomic complexity and diversity of 23 commercial Australian beers. While the overall complexity of the beer proteome was modest, with contributions from barley and yeast proteins, we uncovered a very high diversity of post-translational modifications (PTMs), especially proteolysis, glycation, and glycosylation. Proteolysis was widespread throughout barley proteins, but showed clear site-specificity. Oligohexose modifications were common on lysines in barley proteins, consistent with glycation by maltooligosaccharides released from starch during malting or mashing. O-glycosylation consistent with oligomannose was abundant on secreted yeast glycoproteins. We developed and used data analysis pipelines to efficiently extract and quantify site-specific PTMs from SWATH-MS data, and showed incorporating these features into proteomic analyses extended analytical precision. We found that the key differentiator of the beer glyco/proteome was the brewery, with beer from independent breweries having a distinct profile to beer from multinational breweries. Within a given brewery, beer styles also had distinct glyco/proteomes. Targeting our analyses to beers from a single brewery, Newstead Brewing Co., allowed us to identify beer style-specific features of the glyco/proteome. Specifically, we found that proteins in darker beers tended to have low glycation and high proteolysis. Finally, we objectively quantified features of foam formation and stability, and showed that these quality properties correlated with the concentration of abundant surface-active proteins from barley and yeast.Edward D. KerrChristopher H. CabocheCassandra L. PeggToan K. PhungClaudia Gonzalez ViejoSigfredo FuentesMark T. HowesKate HowellBenjamin L. SchulzNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Medicine R Science Q |
spellingShingle |
Medicine R Science Q Edward D. Kerr Christopher H. Caboche Cassandra L. Pegg Toan K. Phung Claudia Gonzalez Viejo Sigfredo Fuentes Mark T. Howes Kate Howell Benjamin L. Schulz The post-translational modification landscape of commercial beers |
description |
Abstract Beer is one of the most popular beverages worldwide. As a product of variable agricultural ingredients and processes, beer has high molecular complexity. We used DIA/SWATH-MS to investigate the proteomic complexity and diversity of 23 commercial Australian beers. While the overall complexity of the beer proteome was modest, with contributions from barley and yeast proteins, we uncovered a very high diversity of post-translational modifications (PTMs), especially proteolysis, glycation, and glycosylation. Proteolysis was widespread throughout barley proteins, but showed clear site-specificity. Oligohexose modifications were common on lysines in barley proteins, consistent with glycation by maltooligosaccharides released from starch during malting or mashing. O-glycosylation consistent with oligomannose was abundant on secreted yeast glycoproteins. We developed and used data analysis pipelines to efficiently extract and quantify site-specific PTMs from SWATH-MS data, and showed incorporating these features into proteomic analyses extended analytical precision. We found that the key differentiator of the beer glyco/proteome was the brewery, with beer from independent breweries having a distinct profile to beer from multinational breweries. Within a given brewery, beer styles also had distinct glyco/proteomes. Targeting our analyses to beers from a single brewery, Newstead Brewing Co., allowed us to identify beer style-specific features of the glyco/proteome. Specifically, we found that proteins in darker beers tended to have low glycation and high proteolysis. Finally, we objectively quantified features of foam formation and stability, and showed that these quality properties correlated with the concentration of abundant surface-active proteins from barley and yeast. |
format |
article |
author |
Edward D. Kerr Christopher H. Caboche Cassandra L. Pegg Toan K. Phung Claudia Gonzalez Viejo Sigfredo Fuentes Mark T. Howes Kate Howell Benjamin L. Schulz |
author_facet |
Edward D. Kerr Christopher H. Caboche Cassandra L. Pegg Toan K. Phung Claudia Gonzalez Viejo Sigfredo Fuentes Mark T. Howes Kate Howell Benjamin L. Schulz |
author_sort |
Edward D. Kerr |
title |
The post-translational modification landscape of commercial beers |
title_short |
The post-translational modification landscape of commercial beers |
title_full |
The post-translational modification landscape of commercial beers |
title_fullStr |
The post-translational modification landscape of commercial beers |
title_full_unstemmed |
The post-translational modification landscape of commercial beers |
title_sort |
post-translational modification landscape of commercial beers |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/c9d97b75257f40a181f8c3b9b9042c3e |
work_keys_str_mv |
AT edwarddkerr theposttranslationalmodificationlandscapeofcommercialbeers AT christopherhcaboche theposttranslationalmodificationlandscapeofcommercialbeers AT cassandralpegg theposttranslationalmodificationlandscapeofcommercialbeers AT toankphung theposttranslationalmodificationlandscapeofcommercialbeers AT claudiagonzalezviejo theposttranslationalmodificationlandscapeofcommercialbeers AT sigfredofuentes theposttranslationalmodificationlandscapeofcommercialbeers AT markthowes theposttranslationalmodificationlandscapeofcommercialbeers AT katehowell theposttranslationalmodificationlandscapeofcommercialbeers AT benjaminlschulz theposttranslationalmodificationlandscapeofcommercialbeers AT edwarddkerr posttranslationalmodificationlandscapeofcommercialbeers AT christopherhcaboche posttranslationalmodificationlandscapeofcommercialbeers AT cassandralpegg posttranslationalmodificationlandscapeofcommercialbeers AT toankphung posttranslationalmodificationlandscapeofcommercialbeers AT claudiagonzalezviejo posttranslationalmodificationlandscapeofcommercialbeers AT sigfredofuentes posttranslationalmodificationlandscapeofcommercialbeers AT markthowes posttranslationalmodificationlandscapeofcommercialbeers AT katehowell posttranslationalmodificationlandscapeofcommercialbeers AT benjaminlschulz posttranslationalmodificationlandscapeofcommercialbeers |
_version_ |
1718381756780904448 |